| アイテムタイプ |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2024-10-16 |
| タイトル |
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タイトル |
A Proteorhodopsin-Related Photosensor Expands the Repertoire of Structural Motifs Employed by Sensory Rhodopsins |
| 言語 |
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言語 |
eng |
| キーワード |
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主題Scheme |
Other |
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主題 |
Absorption |
| キーワード |
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主題Scheme |
Other |
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主題 |
Acid and base chemistry |
| キーワード |
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主題Scheme |
Other |
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主題 |
Monomers |
| キーワード |
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主題Scheme |
Other |
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主題 |
Peptides and proteins |
| キーワード |
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主題Scheme |
Other |
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主題 |
Reaction mechanisms |
| 資源タイプ |
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資源タイプ |
journal article |
| アクセス権 |
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アクセス権 |
open access |
| 著者 |
Saliminasab, Maryam
山崎, 洋一
Palmateer, Alyssa
Harris, Andrew
Schubert, Luiz
Langner, Pit
Heberle, Joachim
Bondar, Ana-Nicoleta
Brown, Leonid S.
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| 抄録 |
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内容記述タイプ |
Abstract |
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内容記述 |
Microbial rhodopsins are light-activated retinal-binding membrane proteins that perform a variety of ion transport and photosensory functions. They display several cases of convergent evolution where the same function is present in unrelated or very distant protein groups. Here we report another possible case of such convergent evolution, describing the biophysical properties of a new group of sensory rhodopsins. The first representative of this group was identified in 2004 but none of the members had been expressed and characterized. The well-studied haloarchaeal sensory rhodopsins interacting with methyl-accepting Htr transducers are close relatives of the halobacterial proton pump bacteriorhodopsin. In contrast, the sensory rhodopsins we describe here are relatives of proteobacterial proton pumps, proteorhodopsins, but appear to interact with Htr-like transducers likewise, even though they do not conserve the residues important for the interaction of haloarchaeal sensory rhodopsins with their transducers. The new sensory rhodopsins display many unusual amino acid residues, including those around the retinal chromophore; most strikingly, a tyrosine in place of a carboxyl counterion of the retinal Schiff base on helix C. To characterize their unique sequence motifs, we augment the spectroscopy and biochemistry data by structural modeling of the wild-type and three mutants. Taken together, the experimental data, bioinformatics sequence analyses, and structural modeling suggest that the tyrosine/aspartate complex counterion contributes to a complex water-mediated hydrogen-bonding network that couples the protonated retinal Schiff base to an extracellular carboxylic dyad. |
| 書誌情報 |
en : Journal of Physical Chemistry B
巻 127,
号 37,
p. 7872-7886,
発行日 2023-09-11
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| 出版者 |
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出版者 |
American Chemical Society |
| ISSN |
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収録物識別子タイプ |
EISSN |
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収録物識別子 |
1520-5207 |
| 出版者版DOI |
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関連タイプ |
isReplacedBy |
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識別子タイプ |
DOI |
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関連識別子 |
https://doi.org/10.1021/acs.jpcb.3c04032 |
| 出版者版URI |
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関連タイプ |
isReplacedBy |
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識別子タイプ |
URI |
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関連識別子 |
https://pubs.acs.org/doi/10.1021/acs.jpcb.3c04032 |
| 権利 |
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権利情報Resource |
https://creativecommons.org/licenses/by-nc-nd/4.0/ |
|
権利情報 |
Copyright $00A9 2023 The Authors. Published by American Chemical Society. This publication is licensed under CC-BY-NC-ND 4.0 . |
| 著者版フラグ |
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出版タイプ |
NA |
